Bacterial ribosome heterogeneity: Changes in ribosomal protein composition during transition into stationary growth phase.

Bacterial ribosome heterogeneity: Changes in ribosomal protein composition during transition into stationary growth phase. Biochimie. 2018 Oct 22;: Authors: Lilleorg S, Reier K, Pulk A, Liiv A, Tammsalu T, Peil L, Cate JHD, Remme J Abstract Ribosomes consist of many small proteins and few large RNA molecules. Both components are necessary for ribosome functioning during translation. According to widely accepted view, bacterial ribosomes contain always the same complement of ribosomal proteins. Comparative bacterial genomics data indicates that several ribosomal proteins are encoded by multiple paralogous genes suggesting structural heterogeneity of ribosomes. In E. coli, two r-proteins bL31 and bL36 are encoded by two genes: rpmE and ykgM encode bL31 protein paralogs bL31A and bL31B, and rpmJ and ykgO encode bL36 protein paralogs bL36A and bL36B respectively. We have found several similarities and differences between ribosomes of exponential and stationary growth phases by using quantitative mass spectrometry and X-ray crystallography. First, composition of ribosome associating proteins changes profoundly as cells transition from exponential to stationary growth phase. Ribosomal core proteins bL31A and bL36A are replaced by bL31B and bL36B, respectively. Second, our X-ray structure of the 70S ribosome demonstrates that bL31B and bL36B proteins have similar ribosome binding sites to their A counterparts. Third, ribosome subpopulations...
Source: Biochimie - Category: Biochemistry Authors: Tags: Biochimie Source Type: research